Purification and properties of a Triticum aestivum specific albumin

Sodini, G.; Silano, Vittorio; Agazio, M. de; Pocchiari, F.; Tentori, L; Vivaldi, G

doi:10.1016/s0031-9422(00)85304-2

Cited by 30 publications

(9 citation statements)

References 14 publications

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“…Silano et al (1973) reported that five of the six inhibitors they isolated had molecular weights in the range of 14,000 ("0.28" family). The other inhibitor ("0.19") of molecular weight 24,000 (Sodini et al 1970) gave two bands of equally staining intensity on SDS polyacrylamide gels with molecular weights of 13,000 and 14,500 (Silano et al 1973). The molecular weights reported by other workers (Shainkin and Birk 1970;Strumeyer and Fisher 1973;Saunders and Lang 1973) are in general agreement with those reported by Silano et al (1973) and Bedetti et al (1974).…”

Section: Molecular Weight and Subunit Structure Of The Inhibitorsupporting

confidence: 87%

Purification and Some Physical and Chemical Properties of Red Kidney Bean (Phaseolus Vulgaris) ?-Amylase Inhibitor

Powers

Whitaker

1978

J Food Biochemistry

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Red kidney bean contains more amylase inhibitor than do California white bean and cowpea while garbanzo bean and Westan and Westley lima beans do not contain inhibitor. Red kidney bean amylase inhibitor was purified to homogeneity by selective heat treatment (60°C) of a water extract at pH 4. 0, fractionation with ethanol and successive chromatography on DEAE‐ and CM‐cellulose chromatography. The inhibitor has an apparent molecular weight of 49,000 by Sephadex gel filtration and contains 8. 6% carbohydrate probably covalently linked via an amide linkage to asparagine. The inhibitor probably contains four subunits perhaps of three different types. The inhibitor is high in aspartic acid, glutamic acid, serine, threonine and valine, low in cysteine/cystine and does not contain proline. Stable 1:1 complex formation between inhibitor and porcine pancreatic α‐amylase was demonstrated by gel filtration on Sephadex G‐100. The inhibitor has activity against porcine pancreatic α‐amylase, human salivary α‐amylase, and Tenebrio molitor (yellow corn meal worm) larval midgut α‐amylase but is inactive against Bacillus subtilis α‐amylase, Aspergillus oryzae α‐amylase, barley α‐amylase and red kidney bean α‐amylase.

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Section: Molecular Weight and Subunit Structure Of The Inhibitorsupporting

confidence: 87%

Purification and Some Physical and Chemical Properties of Red Kidney Bean (Phaseolus Vulgaris) ?-Amylase Inhibitor

Powers

Whitaker

1978

J Food Biochemistry

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“…6.5, molecular weight 21,000 for 11), but different electrophoretic mobility. AmI, [26], inhibitor I 1311, and 0.19 [30] also showed similar inhibition patterns, almost identical amino acid coqpositions and MW all close to 25,000; this suggests that a 0.19 family of proteins may be present in wheat. All these components were active in inhibiting human salivary and Tenebrio molitor L. alpha-amylase.…”

Section: Characterization and Some Properties Of Multiple Forms Of Cementioning

confidence: 71%

Review article Present‐day studies on cereals protein nature alpha‐amylase inhibitors

Warchalewski¹

1983

Nahrung

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The present state of research on alpha-amylase inhibitors in cereals is reviewed. The detection and assay of alpha-amylase inhibitors, characterization and some properties of multiple forms, as well as their specificities, biochemica1, physiological and nutritional significance are discussed. However insufficient data are available to accurately discuss their implication in food and feed technology. Investigators are initiating furtherstudies to explain these problems.

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“…In 1943, Kneen and Sandstedt discovered a-amylase inhibiting activity in wheat kernel, and in 1976, DePonte et al determined the specific proteins existing in the WA fraction which were responsible for the activity. The specific a-amylase inhibiting proteins were identified as 0.19-, 0.28-, 0.36-, and 0.53-inhibitors according to the results of gel electrophoresis (Sodini et al, 1970). The primary and tertiary structures of these inhibitors were then clarified (Oda et al, 1997;Maeda et al, 1983;Kashlan & Richardson, 1981).…”

Section: Introductionmentioning

confidence: 99%

Effects of single and long-term administration of wheat albumin on blood glucose control: randomized controlled clinical trials

Kodama

Miyazaki²,

Kitamura

et al. 2004

Eur J Clin Nutr

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Objective: To examine the effects of single and long-term administration of wheat albumin (WA) on blood glucose levels and blood glucose control, respectively. Design: Randomly arranged crossover trial for single administration in healthy subjects and double-blinded randomized controlled trial for long-term administration (3 months) in diabetic patients. In vitro a-amylase inhibitory activity of WA was also determined. Setting: Central Research Laboratories of Nisshin Flour Milling Co. Ltd. (Saitama, Japan) for single administration and Aiwa Clinic (Saitama, Japan) for long-term administration. Subjects: A total of 12 healthy adult male volunteers for the single administration and 24 type II outpatient diabetics with mild hyperglycemia for the long-term administration. Interventions: Subjects took soups containing 0, 0.25, 0.5, and 1.0 g WA before test meals for single administration, and patients took soups with or without 0.5 g WA before every meal for the long-term (3 months) administration. Results: In vitro a-amylase inhibitory activity of WA was 150 times that of wheat flour. In the single administration experiment, WA suppressed peak postprandial blood glucose levels in a dose-dependent manner: 31, 47, and 50% reduction after 0.25, 0.5, and 1.0 g administrations, respectively. In the long-term administration, 0.5 g of WA did not affect fasting blood glucose levels, whereas it reduced hemoglobin A 1 c levels. No significant adverse effects such as hypoglycemia or gastrointestinal disturbances were observed in the two experiments. Conclusion: In the treatment of type II diabetic patients, WA might be a useful functional food, which, with diet and exercise, could help to improve blood glucose control without any critical adverse effects.

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Purification and properties of a Triticum aestivum specific albumin

Cited by 30 publications

References 14 publications

Purification and Some Physical and Chemical Properties of Red Kidney Bean (Phaseolus Vulgaris) ?-Amylase Inhibitor

Purification and Some Physical and Chemical Properties of Red Kidney Bean (Phaseolus Vulgaris) ?-Amylase Inhibitor

Review article Present‐day studies on cereals protein nature alpha‐amylase inhibitors

Effects of single and long-term administration of wheat albumin on blood glucose control: randomized controlled clinical trials

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